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Crystal structure of human FPPS in complex with biaryl compound 8e

Analyse Crystal structure of human FPPS in complex with biaryl compound 8e in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5DJV
Type
protein
Length
343 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.3
Source
Homo sapiens
Molecule
Farnesyl pyrophosphate synthase
EC
2.5.1.10, 2.5.1.1
UniProt
P14324
Ligands
5BL
Pockets
1 · best druggability 0.79

Structure

x-ray diffraction · resolution 2.3 · 1 distinct chain · 75% helix, 1% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
FFarnesyl pyrophosphate synthase (EC 2.5.1.10, 2.5.1.1)protein34375% helix, 1% strandP14324

Ligands and binding sites

  • 5BL · 8-(naphthalen-1-yl)-6-(1H-pyrrol-2-yl)quinoline-2-carboxylic acid · ligand · chains F

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19310.790.81675BL

Compared structures

  • 5DJV · Crystal structure of human fpps in complex with biaryl compound 8E · the same entry in another collection · chain F against F, TM-score 1.00
  • P14324 · AlphaFold monomer V2.0 prediction for farnesyl pyrophosphate synthase (P14324) · a predicted model of the same protein · chain F against A, TM-score 0.96

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